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On Promotion
Category
Tested Applications
Conjugation
Biologically Active
Featured Product
Search results for: 'IL-2'
- Active
Item 1 of 1ActiveUnconjugated
95%
17.4 kDa
100 μg, 1 mg - ActiveItem 1 of 1Active
Unconjugated
90%
26.4 kDa
1 mg, 100 μg - ActiveItem 1 of 1Active
Unconjugated
95%
28.3 kDa
1 mg, 100 μg - Featured
Item 1 of 2IL-2 Recombinant Protein [orb1231414]FeaturedELISA, WB
>90% as determined by SDS-PAGE.
17.3 kDa
HEK293 cells
0.1 mg - FeaturedItem 1 of 1Human IL2RA Protein [orb1477817]Featured
Greater than 85% as determined by SDS-PAGE.
50.3 kDa
E.coli
1 mg, 20 μg, 100 μg - FeaturedItem 1 of 1IL2 Protein [orb1476876]Featured
Greater than 90% as determined by SDS-PAGE.
17.0 kDa
Yeast
100 μg, 20 μg, 1 mg - FeaturedItem 1 of 1Human IL2RG Protein [orb1478082]Featured
Greater than 85% as determined by SDS-PAGE.
26.6 kDa
E.coli
20 μg, 1 mg, 100 μg - FeaturedItem 1 of 1Featured
Unconjugated
The purity of the protein is greater than 95% as determined by SDS-PAGE and Coomassie blue staining.
The protein has a predicted molecular mass of 16.2 kDa after removal of the signal peptide.The apparent molecular mass of IL2-His is approximately 15-25 kDa due to glycosylation.
Mammalian
10 μg, 100 μg, 50 μg - FeaturedItem 1 of 1Featured
Unconjugated
The purity of the protein is greater than 95% as determined by SDS-PAGE and Coomassie blue staining.
The protein has a predicted molecular mass of 50.8 kDa after removal of the signal peptide. The apparent molecular mass of mIL2RA-hFc is approximately 70-100 kDa due to glycosylation.
Mammalian
100 μg, 10 μg, 50 μg - FeaturedItem 1 of 1Featured
Greater than 95% as determined by SDS-PAGE.
16.6 kDa
Yeast
1 mg, 100 μg, 20 μg
